INT181186

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Context Info
Confidence 0.35
First Reported 2004
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 78
Total Number 81
Disease Relevance 14.93
Pain Relevance 4.87

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

nucleus (Rxra) enzyme binding (Rxra) DNA binding (Rxra)
transcription factor binding (Rxra)
Anatomy Link Frequency
colon 1
Rxra (Mus musculus)
Pain Link Frequency Relevance Heat
agonist 1330 99.20 Very High Very High Very High
Endocannabinoid 17 97.36 Very High Very High Very High
Cannabinoid 46 96.52 Very High Very High Very High
cytokine 236 95.80 Very High Very High Very High
Inflammation 1221 95.40 Very High Very High Very High
Inflammatory response 138 94.00 High High
Potency 7 93.76 High High
antagonist 165 90.56 High High
aspirin 23 74.80 Quite High
tolerance 23 69.16 Quite High
Disease Link Frequency Relevance Heat
Cardiovascular Disease 36 99.92 Very High Very High Very High
Hyperplasia 13 99.52 Very High Very High Very High
Dyslipidemia /

Combined Dyslipidemia

34 98.32 Very High Very High Very High
Rheumatoid Arthritis 201 95.72 Very High Very High Very High
INFLAMMATION 1458 95.40 Very High Very High Very High
Osteogenic Sarcomas 245 95.12 Very High Very High Very High
Inflammatory Bowel Disease 97 94.92 High High
Apoptosis 353 94.64 High High
Cancer 1005 93.12 High High
Metabolic Disorder 33 92.00 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Rifampicin/PXR/RXRa subsequently binds to a xenobiotic response element (XRE) composed of the direct repeat of alpha and beta half-sites separated by four nucleotides on the CYP3A4 gene, thereby upregulating its expression in phase 1 [28].
RXRa Binding (binds) of
1) Confidence 0.35 Published 2009 Journal PPAR Research Section Body Doc Link PMC2768028 Disease Relevance 0.08 Pain Relevance 0.05
specific pathways [8], with the combination of RXR and PPAR
RXR Binding (combination) of
2) Confidence 0.34 Published 2006 Journal PPAR Research Section Body Doc Link PMC1664714 Disease Relevance 0.28 Pain Relevance 0.31
Cross-talk through DNA binding and RXR heterodimerization present challenges to the study of these nuclear receptors that cannot be adequately addressed by current experimental approaches.
RXR Binding (binding) of
3) Confidence 0.25 Published 2009 Journal PPAR Research Section Abstract Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
At the level of DNA binding, most RXR heterodimers bind selectively to the well-known “DR1 to 5” DNA response elements.
RXR Binding (bind) of
4) Confidence 0.25 Published 2009 Journal PPAR Research Section Abstract Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Early studies showed that deletion of the RXR LBD from amino acid position 443 to the C-terminal end does not disrupt dimerization [56], while additional deletion to position 433 disrupts RXR homodimerization but not heterodimerization with other NRs.
RXR Neg (not) Binding (homodimerization) of
5) Confidence 0.25 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Since each heterodimer possesses different heterodimerization interface, it is reasonable to conjecture that some partners can form more stable heterodimers with RXR than can others, even though the relative stability of each heterodimer is yet to be fully established.
RXR Binding (heterodimers) of
6) Confidence 0.25 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
In addition, other mutations can alter heterodimerization of RXR with certain partners.
RXR Binding (heterodimerization) of
7) Confidence 0.25 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
with RXR) and PPAR?
RXR Binding (with) of
8) Confidence 0.22 Published 2008 Journal PPAR Research Section Body Doc Link PMC2266973 Disease Relevance 0.09 Pain Relevance 0
It has been suggested that the quantity of RXR available for heterodimerization is limited and under strict control [48, 49].
RXR Binding (heterodimerization) of
9) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Nevertheless, the specificity of RXR/PPAR heterodimer to PPRE does not necessarily preclude DNA binding by other RXR heterodimers that also recognize the DR1 element.

3.

RXR Binding (binding) of
10) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Our laboratory has created and tested an engineered RXR/PPAR heterodimer consist of mouse RXR?
RXR Binding (heterodimer) of
11) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0.07 Pain Relevance 0.03
These mutations include RXR A416D or R421L, which specifically disrupt the formation of the RXR/TR heterodimer, and RXR A416K, which disrupts RXR/RAR and RXR/TR [58].
RXR Binding (formation) of
12) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Nevertheless, the specificity of RXR/PPAR heterodimer to PPRE does not necessarily preclude DNA binding by other RXR heterodimers that also recognize the DR1 element.

3.

RXR Binding (specificity) of
13) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
A novel experimental approach is currently being developed to alter the dimerization properties of selected heterodimers, which will allow future studies to dissect a specific RXR heterodimer and its signaling pathway from the rest of the RXR-dependent signaling network.



RXR Binding (heterodimer) of
14) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Interestingly, RAR acquires the heterodimerization properties of RXR when its I-box is replaced by that of the RXR, and vice versa [57].
RXR Binding (heterodimerization) of
15) Confidence 0.19 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Most RXR/partner heterodimers recognize and bind to direct repeat (DR) DNA sequences as their response element [18–23].
RXR Binding (bind) of
16) Confidence 0.18 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
A well-known example is that the RXR homodimer and several other RXR heterodimers can recognize and bind to the DR1 element [29].
RXR Binding (recognize) of
17) Confidence 0.18 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Most RXR/partner heterodimers recognize and bind to direct repeat (DR) DNA sequences as their response element [18–23].
RXR Binding (recognize) of
18) Confidence 0.18 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
Overall, these studies identify the I-box as a crucial element for RXR heterodimerization, and mutations at this region can alter heterodimerization properties.


RXR Binding (heterodimerization) of
19) Confidence 0.18 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0
For instance, although the RXR-RAR heterodimer binds to both DR1 and DR5, the RXR monomer occupies the 3?
RXR Binding (binds) of
20) Confidence 0.18 Published 2009 Journal PPAR Research Section Body Doc Link PMC2801013 Disease Relevance 0 Pain Relevance 0

General Comments

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